KEGG   ENZYME: 1.1.1.282
Entry
EC 1.1.1.282                Enzyme                                 
Name
quinate/shikimate dehydrogenase [NAD(P)+];
YdiB;
quinate/shikimate dehydrogenase (ambiguous)
Class
Oxidoreductases;
Acting on the CH-OH group of donors;
With NAD+ or NADP+ as acceptor
Sysname
L-quinate:NAD(P)+ 3-oxidoreductase
Reaction(IUBMB)
(1) L-quinate + NAD(P)+ = 3-dehydroquinate + NAD(P)H + H+ [RN:R01872 R06846];
(2) shikimate + NAD(P)+ = 3-dehydroshikimate + NAD(P)H + H+ [RN:R02413 R06847]
Reaction(KEGG)
Substrate
L-quinate [CPD:C00296];
NAD+ [CPD:C00003];
NADP+ [CPD:C00006];
shikimate [CPD:C00493]
Product
3-dehydroquinate [CPD:C00944];
NADH [CPD:C00004];
NADPH [CPD:C00005];
H+ [CPD:C00080];
3-dehydroshikimate [CPD:C02637]
Comment
This is the second shikimate dehydrogenase enzyme found in Escherichia coli. It can use both quinate and shikimate as substrates and either NAD+ or NADP+ as acceptor. The low catalytic efficiency with both quinate and shikimate suggests that neither may be the physiological substrate. cf. EC 1.1.1.24, quinate/shikimate dehydrogenase (NAD+), EC 1.1.5.8, quinate/shikimate dehydrogenase (quinone), and EC 1.1.1.25, shikimate dehydrogenase (NADP+).
History
EC 1.1.1.282 created 2004, modified 2021
Pathway
ec00400  Phenylalanine, tyrosine and tryptophan biosynthesis
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
Orthology
K05887  quinate/shikimate dehydrogenase
Genes
ECOb1692(ydiB)
ECJJW1682(ydiB)
ECDECDH10B_1828(ydiB)
EBWBWG_1506(ydiB)
ECOKECMDS42_1365(ydiB)
ECEZ2720(ydiB)
ECSECs_2399(ydiB)
ECFECH74115_2408
ETWECSP_2259(ydiB)
ELXCDCO157_2233(aroE)
EOIECO111_2161(ydiB)
EOJECO26_2420(ydiB)
EOHECO103_1835(ydiB)
ECOOECRM13514_2187(aroE)
ECOHECRM13516_2092(aroE)
ESLO3K_11775
ESOO3O_13860
ESMO3M_11740
ECKEC55989_1859(ydiB)
ECGE2348C_1777(ydiB)
EOKG2583_2089(ydiB)
ELRECO55CA74_10255
ELHETEC_1725
ECWEcE24377A_1908
EUNUMNK88_2155
ECPECP_1639
ENAECNA114_1739(ydiB)
ECOSEC958_1912(ydiB)
ECVAPECO1_768(ydiB)
ECOAAPECO78_12280
ECXEcHS_A1773
ECMEcSMS35_1504
ECYECSE_1815
ECRECIAI1_1745(ydiB)
ECQECED1_1891(ydiB)
EUMECUMN_1981(ydiB)
ECTECIAI39_1366(ydiB)
EOCCE10_1966(ydiB)
EBRECB_01661(ydiB)
EBLECD_01661(ydiB)
EBEB21_01650(ydiB)
EBDECBD_1954
ECIUTI89_C1884(ydiB)
EIHECOK1_1812
ECZECS88_1742(ydiB)
ECCc2087(ydiB)
ELOEC042_1859
ELNNRG857_08475
ESEECSF_1552
ECLEcolC_1939
EKOEKO11_2083
EKFKO11_14285(ydiB)
EABECABU_c19460(ydiB)
EDHEcDH1_1950
EDJECDH1ME8569_1636(ydiB)
ELUUM146_08690
ELWECW_m1861(ydiB)
ELLWFL_09110(ydiB)
ELCi14_1909(aroE)
ELDi02_1909(aroE)
ELPP12B_c1391(aroE)
ELFLF82_2870(ydiB)
ECOLLY180_08815
ECOIECOPMV1_01791(ydiB)
ECOJP423_09035
EALEAKF1_ch4359c
EMAC1192_03790
ESZFEM44_23400(ydiB)
STMSTM1359(ydiB)
SEOSTM14_1650(aroE_1)
SEVSTMMW_13661
SEYSL1344_1293(aroE)
SEMSTMDT12_C13760
SEJSTMUK_1326(aroE)
SEBSTM474_1364(aroE)
SEFUMN798_1416(aroE)
SETUSTU288_03120
SETCCFSAN001921_10345
SENRSTMDT2_12921(aroE)
SENDDT104_13371(aroE)
SENICY43_06920
SEENSE451236_12665
SPQSPAB_01974
SEISPC_2371(aroE)
SECSCH_1378(ydiB)
SEHSeHA_C1490
SHBSU5_01977
SENHCFSAN002069_02210
SEEHSEEH1578_16025
SEESNSL254_A1471
SENNSN31241_24320
SEWSeSA_A1455
SEASeAg_B1813
SENSQ786_08455
SEDSeD_A1984
SEGSG1757(ydiB)
SELSPUL_1177(ydiB)
SEGASPUCDC_1177(ydiB)
SETSEN1685(ydiB)
SENAAU38_08725
SENOAU37_08730
SENVAU39_08735
SENQAU40_09735
SENLIY59_08920
SENJCFSAN001992_04800
SEECCFSAN002050_13185
SEEBSEEB0189_012740
SEEPI137_05420
SENBBN855_13970
SENEIA1_06705
SENCSEET0819_13440
SALZEOS98_12675
SFLSF1722(aroE)
SFXS1854(ydiB)
SFVSFV_1718(ydiB)
SFESFxv_1929(ydiB)
SFNSFy_2467
SFSSFyv_2522
SFTNCTC1_01868(ydiB)
SSNSSON_1462(ydiB)
SBCSbBS512_E1895
SDYSDY_1475(ydiB)
SDZAsd1617_01960
SHQA0259_12505
ENFAKI40_1900(ydiB)
CFDCFNIH1_16775
CBRAA6J81_02970
CWECO701_11460
CYOCD187_13335
CPOTFOB25_01110(ydiB)
CFQC2U38_13295
CAMAF384_06180
CAFAL524_16140
CIFAL515_11000
CFARCI104_12065
CIRC2U53_21260
CIEAN232_19085
CPARCUC49_06605
CTELGBC03_18520(ydiB)
CITZE4Z61_03985(ydiB)
CARSE1B03_12065(ydiB)
KRDA3780_14345
SYMK6K13_13495(ydiB)
YAKACZ76_17775
YMADA391_12680
SFWWN53_13740
SFGAV650_09345
SERASer39006_011055
SERQCWC46_11050
DDCDd586_0792
DZCW909_03900
DDADd703_1385
BGJAWC36_00935
BIZHC231_04870(ydiB)
SUTKFG381_00155(ydiB)
SWSI6J16_03205(ydiB)
LMOEBN418_0563
LMOBBN419_0569
 » show all
Reference
1  [PMID:12637497]
  Authors
Michel G, Roszak AW, Sauve V, Maclean J, Matte A, Coggins JR, Cygler M, Lapthorn AJ
  Title
Structures of shikimate dehydrogenase AroE and its Paralog YdiB. A common structural framework for different activities.
  Journal
J Biol Chem 278:19463-72 (2003)
DOI:10.1074/jbc.M300794200
  Sequence
[eco:b1692]
Reference
2  [PMID:12624088]
  Authors
Benach J, Lee I, Edstrom W, Kuzin AP, Chiang Y, Acton TB, Montelione GT, Hunt JF.
  Title
The 2.3-A crystal structure of the shikimate 5-dehydrogenase orthologue YdiB from Escherichia coli suggests a novel catalytic environment for an NAD-dependent dehydrogenase.
  Journal
J Biol Chem 278:19176-82 (2003)
DOI:10.1074/jbc.M301348200
  Sequence
[eco:b1692]
Other DBs
ExplorEnz - The Enzyme Database: 1.1.1.282
IUBMB Enzyme Nomenclature: 1.1.1.282
ExPASy - ENZYME nomenclature database: 1.1.1.282
BRENDA, the Enzyme Database: 1.1.1.282

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